A study of the development of adenovirus antigens by the immunofluorescent technique

Hayashi, Kaoru; Russell, W. C.

doi:10.1016/0042-6822(68)90067-6

Cited by 37 publications

(20 citation statements)

References 14 publications

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“…protein V could be detected in the nucleus as small aggregates proximal to the nuclear membrane and then in the form of large prominent nucleolar-like rings -in some cases only one large ring was observed. These rings were quite distinct from the early nonstructural protein, the DNA-binding protein, which assembles in characteristic patterns as previously described (Hayashi & Russell, 1968) (see Fig. 2 c, d).…”

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Adenovirus core protein V is delivered by the invading virus to the nucleus of the infected cell and later in infection is associated with nucleoli.

Matthews

Russell

1998

Journal of General Virology

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A ' west-Western ' blotting procedure indicates that adenovirus core protein V is linked to the capsid via protein VI. Double-labelling techniques employing confocal microscopy and immunofluorescence suggest that this linkage is disrupted following infection and penetration of the host cell. Protein V enters the nucleus presumably still in association with the other core proteins attached to the virus genome. Later in infection protein V rapidly accumulates in the nucleus in close association with nucleoli.Virus capsid proteins play a key role in the recognition of cell receptors and consequential adsorption and penetration of the virus. In the case of adenoviruses there is a complex capsid structure comprising seven different proteins. The major capsomere is the hexon of which there are 240, forming an icosahedral shell with the 12 apices of the icosahedron accommodating pentons which are themselves bipartite, consisting of the penton base and fibre. A number of other proteins, viz. VI, VIII, IIIa and IX, interact to stabilize this structure and to contact the nucleoprotein core of the virus. The latter consists of a linear double-stranded DNA genome, with a covalently linked terminal protein (TP) at each 5h terminus, in close association with the highly basic protein VII and a more loosely associated protein V. The locations of the major components of the capsid have been well-defined and tentative assignments have been made for the other capsid proteins based on cryoelectron microscopy and knowledge of the structure of the hexon from X-ray analysis (Stewart et al., 1993). The disposition of the core proteins is not so wellestablished but there have been indications that the genome is held in a tightly coiled configuration. A number of these

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Adenovirus core protein V is delivered by the invading virus to the nucleus of the infected cell and later in infection is associated with nucleoli.

Matthews

Russell

1998

Journal of General Virology

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“…MGBG could prevent the induction of thymidine kinase by AdS by interfering with the expression of adenovirus early genes. We tested this possibility by staining drug-treated infected cells with P antiserum, which reacts with adenovirus early proteins (5). No difference in the number of cells scored as positive for P antigen was obtained between MGBG-treated and untreated cells, despite a large inhibition by MGBG of thymidine kinase induction in this experiment (Table 2).…”

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Adenovirus type 5 induces progression of quiescent rat cells into S phase without polyamine accumulation.

Cheetham¹,

Shaw²,

Bellett³

1982

Mol. Cell. Biol.

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Adenovirus type S induces cellular DNA synthesis and thymidine kinase in quiescent rat cells but does not induce ornithine decarboxylase. We now show that unlike serum, adenovirus type 5 fails to induce S-adenosylmethionine decarboxylase or polyamine accumulation. The inhibition by methylglyoxal bis(guanylhydrazone) of the induction of thymidine kinase by adenovirus type 5 is probably unrelated to its effects on polyamine biosynthesis. Thus, induction of cellular thymidine kinase and DNA replication by adenovirus type 5 is uncoupled from polyamine accumulation.Rat embryo fibroblasts cultured in medium with 0.2% serum become quiescent and arrested in the Gl phase of the cell cycle. The addition of fresh medium containing 10% serum initiates a series of biochemical events which lead to DNA synthesis and cell division. Infection of quiescent rat cells by adenovirus type 5 (Ad5) also induces cellular DNA synthesis (3) and thymidine kinase (3a), an enzyme whose activity increases as the cells enter S phase (16).The induction of DNA synthesis is preceded by the induction of ornithine decarboxylase and S-adenosylmethionine decarboxylase, two key enzymes of polyamine biosynthesis, in a wide variety of systems (17). Further, inhibitors of these two enzymes inhibit subsequent DNA synthesis under several different conditions (2,(7)(8)(9)18). It thus appears that polyamine accumulation in Gl is necessary for the entry of quiescent cells into S phase.AdS, however, differs from serum in that it induces cellular thymidine kinase and DNA synthesis without inducing ornithine decarboxylase (3a). Further, the induction of thymidine kinase by AdS, unlike its induction by serum, is not inhibited by ox-methylornithine, an inhibitor of ornithine decarboxylase (3a). Methylglyoxal bis(guanylhydrazone) (MGBG), an inhibitor of S-adenosylmethionine decarboxylase, inhibits the induction of thymidine kinase by t Present address:

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“…Our experiments have shown that these structures are probably the sites of accumulation of the arginine-rich basic proteins which appear to be of crucial importance in adenovirus infection. In the absence of arginine in the tissue culture medium adenovirus fails to mature and the fluorescent rings and balls characteristic of the later form of the P antigen do not appear (Hayashi & Russell, 1968;Russell & Becker, 1968). The findings that adenovirus contains at least one component of the P antigen and that there is a polypeptide very rich in arginine in association with the virus DNA (Russell & Knight, 1967;Russell et al I97I) suggest that the later form of the P antigen as characterized by the fluorescent rings and rosettes is indeed related to the internal arginine-rich virus nucleoprotein.…”

Section: Discussionmentioning

confidence: 99%

“…Staining of parallel coverslip cultures of adenovirus-infected HEK cells, by the indirect method using a rabbit antiserum against P antigen, was as described previously (Hayashi & Russell, 1968). Specimens were examined by dark-field fluorescence microscopy with blue-violet excitation.…”

Section: Fluorescent Antibody Techniquementioning

confidence: 99%

A Cytochemical Study of Basic Proteins in Adenovirus-infected Cells

Russell¹,

Brodaty²,

Armstrong³

1971

Journal of General Virology

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SUMMARYOn staining adenovirus-infected cells with phenanthrenequinone and with copper phthalocyanin-neutral red, characteristic structures in the form of rings and rosettes were observed. These structures could also be visualized by phase-contrast microscopy and by fluorescent antibody staining with adenovirus P antiserum. The cytochemical staining could be blocked by pre-treatment of the fixed cells with benzil, and the result suggested that the rings and rosettes were the sites of accumulation of arginine-rich basic proteins.

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A study of the development of adenovirus antigens by the immunofluorescent technique

Cited by 37 publications

References 14 publications

Adenovirus core protein V is delivered by the invading virus to the nucleus of the infected cell and later in infection is associated with nucleoli.

Adenovirus core protein V is delivered by the invading virus to the nucleus of the infected cell and later in infection is associated with nucleoli.

Adenovirus type 5 induces progression of quiescent rat cells into S phase without polyamine accumulation.

A Cytochemical Study of Basic Proteins in Adenovirus-infected Cells

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